The nucleoporin Seh1 forms a complex with Mio and serves an essential tissue-specific function in Drosophila oogenesis.
- Citation data:
Development (Cambridge, England), ISSN: 1477-9129, Vol: 138, Issue: 10, Page: 2133-42
- Publication Year:
- Repository URL:
- 10.1242/dev.057372; 10.3410/f.10275956.11073054
- Biochemistry, Genetics and Molecular Biology; Seh1 (Nup44A); Mio; NPC; Nup107-160; Nucleoporin; Oogenesis; Meiosis; Germline; Drosophila; Mtor (Tpr); Microtubule; Animals; Base Sequence; DNA Primers; Drosophila Proteins; Drosophila melanogaster; Female; Gene Expression Regulation, Developmental; Gene Knockout Techniques; Genes, Insect; Multiprotein Complexes; Nuclear Pore Complex Proteins; Nuclear Proteins; Oogenesis; RNA Interference; TOR Serine-Threonine Kinases; Tissue Distribution; Cell Biology; Developmental Biology; Molecular Biology; Molecular Genetics; Musculoskeletal Diseases; Nervous System Diseases
The nuclear pore complex (NPC) mediates the transport of macromolecules between the nucleus and cytoplasm. Recent evidence indicates that structural nucleoporins, the building blocks of the NPC, have a variety of unanticipated cellular functions. Here, we report an unexpected tissue-specific requirement for the structural nucleoporin Seh1 during Drosophila oogenesis. Seh1 is a component of the Nup107-160 complex, the major structural subcomplex of the NPC. We demonstrate that Seh1 associates with the product of the missing oocyte (mio) gene. In Drosophila, mio regulates nuclear architecture and meiotic progression in early ovarian cysts. Like mio, seh1 has a crucial germline function during oogenesis. In both mio and seh1 mutant ovaries, a fraction of oocytes fail to maintain the meiotic cycle and develop as pseudo-nurse cells. Moreover, the accumulation of Mio protein is greatly diminished in the seh1 mutant background. Surprisingly, our characterization of a seh1 null allele indicates that, although required in the female germline, seh1 is dispensable for the development of somatic tissues. Our work represents the first examination of seh1 function within the context of a multicellular organism. In summary, our studies demonstrate that Mio is a novel interacting partner of the conserved nucleoporin Seh1 and add to the growing body of evidence that structural nucleoporins can have novel tissue-specific roles.